| IED ID | IndEnz0002003805 |
| Enzyme Type ID | protease003805 |
| Protein Name |
Putative N-acetylated-alpha-linked acidic dipeptidase NAALADase EC 3.4.-.- Cell growth-inhibiting gene 26 protein Prostate-specific membrane antigen-like protein Putative folate hydrolase 1B |
| Gene Name | FOLH1B PSMAL GIG26 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGGSAPPDSSWRGSLKVSYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHETVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEDNSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYNISMKHPQEMKTYSLSFDSLFSAVKNFTEIASKFSERLQDFDKSNPILLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGDVKRQISVAAFTVQAAAETLSEVA |
| Enzyme Length | 442 |
| Uniprot Accession Number | Q9HBA9 |
| Absorption | |
| Active Site | ACT_SITE 116; /note=For NAALADase activity; /evidence=ECO:0000250; ACT_SITE 320; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 358; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 381; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 116; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; BINDING 211; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04609; BINDING 244; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q04609 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. {ECO:0000250}.; FUNCTION: Exhibits a dipeptidyl-peptidase IV type activity. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Binding site (3); Chain (1); Glycosylation (5); Metal binding (9); Natural variant (1); Region (4) |
| Keywords | Cytoplasm;Dipeptidase;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Multifunctional enzyme;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14716746}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10085079; 16467855; 19678840; 22304711; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,045 |
| Kinetics | |
| Metal Binding | METAL 69; /note=Zinc 1; /evidence=ECO:0000250; METAL 69; /note=Zinc 1; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 79; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 79; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 117; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 125; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 128; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q04609; METAL 145; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:Q9Y3Q0; METAL 245; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q04609 |
| Rhea ID | |
| Cross Reference Brenda |